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Mutations and differential expression of several GalNAc-Ts are associated with many disease states including cancers. The mechanisms by which these isozymes choose their targets and their roles in disease are not fully understood. We previously showed that the GalNAc-Ts possess common and unique specificities for acceptor type, peptide sequence and prior neighboring, and\/or remote substrate GalNAc glycosylation. In the present study, the role of flanking charged residues was investigated using a library of charged peptide substrates containing the central -YAVTPGP- acceptor sequence. Eleven human and one bird GalNAc-T were initially characterized revealing a range of preferences for net positive, net negative, or unique combinations of flanking N- and\/or C-terminal charge, correlating to each isozyme\u2019s different electrostatic surface potential. It was further found that isoforms with high sequence identity (&amp;gt;70%) within a subfamily can possess vastly different charge specificities. Enzyme kinetics, activities obtained at elevated ionic strength, and molecular dynamics simulations confirm that the GalNAc-Ts differently recognize substrate charge outside the common +\/\u22123 residue binding site. These electrostatic interactions impact how charged peptide substrates bind\/orient on the transferase surface, thus modulating their activities. In summary, we show the GalNAc-Ts utilize more extended surfaces than initially thought for binding substrates based on electrostatic, and likely other hydrophobic\/hydrophilic interactions, furthering our understanding of how these transferases select their target.<\/jats:p>","DOI":"10.1093\/glycob\/cwad066","type":"journal-article","created":{"date-parts":[[2023,8,9]],"date-time":"2023-08-09T13:15:33Z","timestamp":1691586933000},"page":"817-836","source":"Crossref","is-referenced-by-count":14,"title":["Polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) isozyme surface charge governs charge substrate preferences to modulate mucin type O-glycosylation"],"prefix":"10.1093","volume":"33","author":[{"given":"Collin J","family":"Ballard","sequence":"first","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland, OH 44106 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miya 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Molecular Medicine, Faculty of Health Sciences, , Blegdamsvej 3, DK-2200 Copenhagen , Denmark"},{"name":"Fundaci\u00f3n ARAID , Zaragoza 50018 , Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas A","family":"Gerken","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Case Western Reserve University , Cleveland, OH 44106 , USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2023,8,9]]},"reference":[{"issue":"10","key":"2023110719284264500_ref1","doi-asserted-by":"crossref","first-page":"4852","DOI":"10.1021\/acs.jcim.1c00998","article-title":"Making it rain: cloud-based molecular simulations for everyone","volume":"61","author":"Arantes","year":"2021","journal-title":"J Chem Inf Model"},{"issue":"7","key":"2023110719284264500_ref2","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1093\/glycob\/cwy021","article-title":"Global aspects of viral 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